ArticlePlant physiology2005
Cloning and functional characterization of a formin-like protein (AtFH8) from Arabidopsis.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Genome-wide identification and gene expression analysis of Formin homology 2 (FH2) genes in peanut.BMC plant biology · 2026Article
- Cytoskeletal control of development and environmental adaptation in plants.Science China. Life sciences · 2026Review
- Population structure of wild and cultivated grapevines in Armenia.BMC plant biology · 2026Article
- Article
- Genome-Wide Characterization and Analysis of theGenes · 2025Article
- Article
- Transmembrane formins as active cargoes of membrane trafficking.Journal of experimental botany · 2024Review
- CHLOROPLAST UNUSUAL POSITIONING 1 is a plant-specific actin polymerization factor regulating chloroplast movement.The Plant cell · 2024Article
- Comparative transcriptome analysis of Zea mays upon mechanical wounding.Molecular biology reports · 2023Article
- Formin protein DRT1 affects gross morphology and chloroplast relocation in rice.Plant physiology · 2023Article
- Actin depolymerizing factor ADF7 inhibits actin bundling protein VILLIN1 to regulate root hair formation in response to osmotic stress in Arabidopsis.PLoS genetics · 2022Article
- Article
- Comprehensive analysis of formin gene family highlights candidate genes related to pollen cytoskeleton and male fertility in wheat (Triticum aestivum L.).BMC genomics · 2021Article
- Formin-mediated bridging of cell wall, plasma membrane, and cytoskeleton in symbiotic infections of Medicago truncatula.Current biology : CB · 2021Article
- Analysis of formin functions during cytokinesis using specific inhibitor SMIFH2.Plant physiology · 2021Article
- TheFrontiers in plant science · 2021Article
- GLABRA2 Regulates Actin Bundling Protein VILLIN1 in Root Hair Growth in Response to Osmotic Stress.Plant physiology · 2020Article
- The Nanoscale Organization of the Plasma Membrane and Its Importance in Signaling: A Proteolipid Perspective.Plant physiology · 2020Review
- Exogenous Nitro-Oleic Acid Treatment Inhibits Primary Root Growth by Reducing the Mitosis in the Meristem inFrontiers in plant science · 2020Article
- Genome-Wide Association Study for Squalene Contents and Functional Haplotype Analysis in Rice.ACS omega · 2019Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The actin cytoskeleton is required for many cellular processes in plant cells. The nucleation process is the rate-limiting step for actin assembly. Formins belong to a new class of conserved actin nucleator, which includes at least 2 formin homology domains, FH1 and FH2, which direct the assembly of unbranched actin filaments. The function of plant formins is quite poorly understood. Here, we provide the first biochemical study of the function of conserved domains of a formin-like protein (AtFH8) from Arabidopsis (Arabidopsis thaliana). The purified recombinant AtFH8(FH1FH2) domain has the ability to nucleate actin filaments in vitro at the barbed end and caps the barbed end of actin filaments, decreasing the rate of subunit addition and dissociation. In addition, purified AtFH8(FH1FH2) binds actin filaments and severs them into short fragments. The proline-rich domain (FH1) of the AtFH8 binds directly to profilin and is necessary for nucleation when actin monomers are profilin bound. However, profilin inhibits the nucleation mediated by AtFH8(FH1FH2) to some extent, but increases the rate of actin filament elongation in the presence of AtFH8(FH1FH2). Moreover, overexpression of the full-length AtFH8 in Arabidopsis causes a prominent change in root hair cell development and its actin organization, indicating the involvement of AtFH8 in polarized cell growth through the actin cytoskeleton.
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